ArticleProteins2013
Sequence recombination improves target specificity in a redesigned collagen peptide abc-type heterotrimer.
Article in Proteins, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- De Novo Design of Specific Heterotrimeric Collagen-Like Peptides via Genetic Algorithm.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Around the collagen triple helix: an introduction to studying associated genetic and acquired diseases.Matrix biology : journal of the International Society for Matrix Biology · 2025Review
- Predicting the stability of homotrimeric and heterotrimeric collagen helices.Nature chemistry · 2021Article
- Empirical estimation of local dielectric constants: Toward atomistic design of collagen mimetic peptides.Biopolymers · 2015Article
- Neighbor preferences of amino acids and context-dependent effects of amino acid substitutions in human, mouse, and dog.International journal of molecular sciences · 2014Article
- Design of net-charged abc-type collagen heterotrimers.Journal of structural biology · 2014Article
- Control of Collagen Stability and Heterotrimer Specificity through Repulsive Electrostatic Interactions.Biomolecules · 2013Article
- Circular permutation directs orthogonal assembly in complex collagen peptide mixtures.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Stability of the collagen triple helix is largely governed by its imino acid content, namely the occurrence of proline and 4R-hydroxyproline at the X and Y positions, respectively, of the periodic (Gly-X-Y)(n) sequence. Although other amino acids at these positions reduce stability of the triple helix, this can be partially compensated by introducing intermolecular side-chain salt bridges. This approach was previously used to design an abc-type heterotrimer composed of one basic, one acidic, and one neutral imino acid rich chain (Gauba and Hartgerink, J Am Chem Soc 2007;129:15034-15041). In this study, an abc-type heterotrimer was designed to be the most stable species using a sequence recombination strategy that preserved both the amino acid composition and the network of interchain salt bridges of the original design. The target heterotrimer had the highest T(m) of 50 °C, 7 °C greater than the next most stable species. Stability of the heterotrimer decreased with increasing ionic strength, consistent with the role of intermolecular salt bridges in promoting stability. Quantitative meta-analysis of these results and published stability measurements on closely related peptides was used to discriminate the contributions of backbone propensity and side-chain electrostatics to collagen stability.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.